The 4-stranded helical arrangement of myosin heads on insect (Lethocerus) flight muscle thick filaments

Morris, Edward P.; Squire, John M.; Fuller, Gary W.

doi:10.1016/1047-8477(91)90049-3

Cited by 51 publications

(50 citation statements)

References 29 publications

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“…7C, a prediction also made by more realistic, detailed models Reedy, 1978,1984). This prediction is exactly borne out by studies which look in close detail at the shape of the rigor cross-bridges across the unit cell, which show not only changes in cross-bridge shape (Reedy et al, 1983b;Morris et al, 1991;Taylor et al, 1993;Chen et al, 2002;Liu et al, ,2006 and number (Taylor et al, 1993), but also that lead cross bridges containing only a single head, and rear cross-bridges containing two heads, are also present (Chen et al, 2002).…”

Section: Actin-myosin Interaction and Force Generationmentioning

confidence: 81%

“…6A6) are now known to have a four fold rotational symmetry and helix structure (off meriodonal reflections 38.5 and 23.3 nm) and diameter (23.5 nm) similar to those of chelicerate thick filaments (Fig. 6A1) (Reedy et al, 1981(Reedy et al, , 1992Goody et al, 1985;Beinbrech et al, 1985;Hinkel-Aust et al, 1990;Ménétret et al, 1990;Morris et al, 1991;Schmitz et al, 1994b;Al Khayat et al, 2004a). The altered crown rotation results in this filament's heads coming back into register every 8 crowns (116 nm) instead of every 3 (43.5 nm).…”

Section: 23mentioning

confidence: 97%

“…The altered crown rotation results in this filament's heads coming back into register every 8 crowns (116 nm) instead of every 3 (43.5 nm). Although enough head mass continues to point along the right handed helices that the filaments have a right handed appearance (Morris et al, 1991), most of the mass of the pairs of myosin heads extends circumferentially around the crowns. Instead of strong strands like the other filaments, this thick filament thus instead has rings around it (Levine, 1997).…”

Section: 23mentioning

confidence: 99%

“…Asynchronous flight muscle-Some muscle thin and thick filaments, however, are organized with great regularity. Insect asynchronous flight muscle is a particularly well studied example (Reedy, 1967(Reedy, , 1968Reedy et al, 1973Reedy et al, , 1981Reedy et al, , 1993Heuser, 1983;Morris et al, 1991). Great care must be taken in reading this literature.…”

Section: Actin-myosin Interaction and Force Generationmentioning

confidence: 99%

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Invertebrate muscles: Thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle

Hooper

Hobbs

Thuma

2008

Progress in Neurobiology

131

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This is the second in a series of canonical reviews on invertebrate muscle. We cover here thin and thick filament structure, the molecular basis of force generation and its regulation, and two special properties of some invertebrate muscle, catch and asynchronous muscle. Invertebrate thin filaments resemble vertebrate thin filaments, although helix structure and tropomyosin arrangement show small differences. Invertebrate thick filaments, alternatively, are very different from vertebrate striated thick filaments and show great variation within invertebrates. Part of this diversity stems from variation in paramyosin content, which is greatly increased in very large diameter invertebrate thick filaments. Other of it arises from relatively small changes in filament backbone structure, which results in filaments with grossly similar myosin head placements (rotating crowns of heads every 14.5 nm) but large changes in detail (distances between heads in azimuthal registration varying from three to thousands of crowns). The lever arm basis of force generation is common to both vetebrates and invertebrates, and in some invertebrates this process is understood on the near atomic level. Invertebrate actomyosin is both thin (tropomyosin:troponin) and thick (primarily via direct Ca ++ binding to myosin) filament regulated, and most invertebrate muscles are dually regulated. These mechanisms are well understood on the molecular level, but the behavioral utility of dual regulation is less so. The phosphorylation state of the thick filament associated giant protein, twitchin, has been recently shown to be the molecular basis of catch. The molecular basis of the stretch activation underlying asynchronous muscle activity, however, remains unresolved.

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Section: Actin-myosin Interaction and Force Generationmentioning

confidence: 81%

Section: 23mentioning

confidence: 97%

Section: 23mentioning

confidence: 99%

Section: Actin-myosin Interaction and Force Generationmentioning

confidence: 99%

See 2 more Smart Citations

Invertebrate muscles: Thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle

Hooper

Hobbs

Thuma

2008

Progress in Neurobiology

131

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“…The number of helices in the thick filaments was found to be either 3 in vertebrates (frog, Kensler and Stewart 1983;rabbit, Kensler and Stewart 1993), 4 in arthropods (Limulus, (Stewart et al 1981;tarantula, Crowther et al 1985;Padrón et al 1993a;and scorpion, Stewart et al 1985) or 7 in mollusks (scallop, Vibert and Craig 1983;Craig et al 1991). Other EM studies on negatively stained thick filaments have been reported for invertebrates such as the indirect flight muscle (IFM) of the giant water bug Lethocerus indicus (Insecta) (Clarke et al 1986;Morris et al 1991), as well as for skeletal muscle in several vertebrates such as goldfish Carassius auratus (Kensler and Stewart 1989;Eakins et al 2002), frog Rana pipiens Stewart and Kensler 1986), chicken (Kensler and Woodhead 1995) and rabbit (Kensler and Stewart 1993). However, none of these studies achieved enough resolution to resolve both heads in the thick filaments 3D reconstruction.…”

Section: Why Tarantula Muscle?mentioning

confidence: 98%

Lessons from a tarantula: new insights into muscle thick filament and myosin interacting-heads motif structure and function

et al. 2017

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The tarantula skeletal muscle X-ray diffraction pattern suggested that the myosin heads were helically arranged on the thick filaments. Electron microscopy (EM) of negatively stained relaxed tarantula thick filaments revealed four helices of heads allowing a helical 3D reconstruction. Due to its low resolution (5.0 nm), the unambiguous interpretation of densities of both heads was not possible. A resolution increase up to 2.5 nm, achieved by cryo-EM of frozen-hydrated relaxed thick filaments and an iterative helical real space reconstruction, allowed the resolving of both heads. The two heads, Bfree^and Bblocked^, formed an asymmetric structure named the Binteracting-heads motif^(IHM) which explained relaxation by self-inhibition of both heads ATPases. This finding made tarantula an exemplar system for thick filament structure and function studies. Heads were shown to be released and disordered by Ca 2+ -activation through myosin regulatory light chain phosphorylation, leading to EM, small angle X-ray diffraction and scattering, and spectroscopic and biochemical studies of the IHM structure and function. The results from these studies have consequent implications for understanding and explaining myosin super-relaxed state and thick filament activation and regulation. A cooperative phosphorylation mechanism for activation in tarantula skeletal muscle, involving swaying constitutively Ser35 mono-phosphorylated free heads, explains super-relaxation, force potentiation and posttetanic potentiation through Ser45 mono-phosphorylated blocked heads. Based on this mechanism, we propose a swaying-swinging, tilting crossbridge-sliding filament for tarantula muscle contraction.

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Structural Analysis of Fibrous Proteins

Scheibel

Serpell

2008

Protein Science Encyclopedia

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Originally published in: Protein Folding Handbook. Part II. Edited by Johannes Buchner and Thomas Kiefhaber. Copyright © 2005 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30784‐2 The sections in this article are Introduction Overview: Protein Fibers Formed in vivo Amyloid Fibers Silks Collagens Actin, Myosin, and Tropomyosin Filaments Intermediate Filaments/Nuclear Lamina Fibrinogen/Fibrin Microtubules Elastic Fibers Flagella and Pili Filamentary Structures in Rod‐like Viruses Protein Fibers Used by Viruses and Bacteriophages to Bind to Their Hosts Overview: Fiber Structures Study of the Structure of β‐sheet‐containing Proteins Amyloid Paired Helical Filaments β‐Silks β‐Sheet‐containing Viral Fibers α‐Helix‐containing Protein Fibers Collagen Tropomyosin Intermediate Filaments Protein Polymers Consisting of a Mixture of Secondary Structure Tubulin Actin and Myosin Filaments Methods to Study Fiber Assembly Circular Dichroism Measurements for Monitoring Structural Changes Upon Fiber Assembly Theory of CD Experimental Guide to Measure CD Spectra and Structural Transition Kinetics Intrinsic Fluorescence Measurements to Analyze Structural Changes Theory of Protein Fluorescence Experimental Guide to Measure Trp Fluorescence Covalent Fluorescent Labeling to Determine Structural Changes of Proteins with Environmentally Sensitive Fluorophores Theory on Environmental Sensitivity of Fluorophores Experimental Guide to Labeling Proteins With Fluorophores 1‐Anilino‐8‐Naphthalensulfonate ( ANS ) Binding to Investigate Fiber Assembly Theory on Using ANS Fluorescence for Detecting Conformational Changes in Proteins Experimental Guide to Using ANS for Monitoring Protein Fiber Assembly Light Scattering to Monitor Particle Growth Theory of Classical Light Scattering Theory of Dynamic Light Scattering Experimental Guide to Analyzing Fiber Assembly Using DLS Field‐flow Fractionation to Monitor Particle Growth Theory of FFF Experimental Guide to Using FFF for Monitoring Fiber Assembly Fiber Growth‐rate Analysis Using Surface Plasmon Resonance Theory of SPR Experimental Guide to Using SPR for Fiber‐growth Analysis Single‐fiber Growth Imaging Using Atomic Force Microscopy Theory of Atomic Force Microscopy Experimental Guide for Using AFM to Investigate Fiber Growth Dyes Specific for Detecting Amyloid Fibers Theory on Congo Red and Thioflavin T Binding to Amyloid Experimental Guide to Detecting Amyloid Fibers with CR and Thioflavin Binding Methods to Study Fiber Morphology and Structure Scanning Electron Microscopy for Examining the Low‐resolution Morphology of a Fiber Specimen Theory of SEM Experimental Guide to Examining Fibers by SEM Transmission Electron Microscopy for Examining Fiber Morphology and Structure Theory of TEM Experimental Guide to Examining Fiber Samples by TEM Cryo‐electron Microscopy for Examination of the Structure of Fibrous Proteins Theory of Cryo‐electron Microscopy Experimental Guide to Preparing Proteins for Cryo‐electron Microscopy Structural Analysis from Electron Micrographs Atomic Force Microscopy for Examining the Structure and Morphology of Fibrous Proteins Experimental Guide for Using AFM to Monitor Fiber Morphology Use of X ‐ray Diffraction for Examining the Structure of Fibrous Proteins Theory of X ‐Ray Fiber Diffraction Experimental Guide to X ‐Ray Fiber Diffraction Fourier Transformed Infrared Spectroscopy Theory of FTIR Experimental Guide to Determining Protein Conformation by FTIR Conclusions Acknowledgements

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The 4-stranded helical arrangement of myosin heads on insect (Lethocerus) flight muscle thick filaments

Cited by 51 publications

References 29 publications

Invertebrate muscles: Thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle

Invertebrate muscles: Thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle

Lessons from a tarantula: new insights into muscle thick filament and myosin interacting-heads motif structure and function

Structural Analysis of Fibrous Proteins

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